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Ectodomain shedding of neuroglycan C, a brain-specific chondroitin sulfate proteoglycan, by TIMP-2- and TIMP-3-sensitive proteolysis.

Authors: Shuo, T  Aono, S  Nakanishi, K  Tokita, Y  Kuroda, Y  Ida, M  Matsui, F  Maruyama, H  Kaji, T  Oohira, A 
Citation: Shuo T, etal., J Neurochem. 2007 Sep;102(5):1561-8. Epub 2007 May 26.
Pubmed: (View Article at PubMed) PMID:17532789
DOI: Full-text: DOI:10.1111/j.1471-4159.2007.04658.x

Neuroglycan C (NGC) is a transmembrane-type of chondroitin sulfate proteoglycan with an epidermal growth factor (EGF)-like module that is exclusively expressed in the CNS. Because ectodomain shedding is a common processing step for many transmembrane proteins, we examined whether NGC was subjected to proteolytic cleavage. Western blotting demonstrated the occurrence of a soluble form of NGC with a 75 kDa core glycoprotein in the soluble fraction of the young rat cerebrum. In contrast, full-length NGC with a 120 kDa core glycoprotein and its cytoplasmic fragment with a molecular size of 35 kDa could be detected in the membrane fraction. The soluble form of NGC was also detectable in culture media of fetal rat neurons, and the full-length form existed in cell layers. The amount of the soluble form in culture media was decreased by adding a physiological protease inhibitor such as a tissue inhibitor of metalloproteinase (TIMP)-2 or TIMP-3, but not by adding TIMP-1. Both EGF-like and neurite outgrowth-promoting activity of the NGC ectodomain may be regulated by this proteolytic processing.


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CRRD Object Information
CRRD ID: 2290425
Created: 2008-03-12
Species: All species
Last Modified: 2008-03-12
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.